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Biomedical subjects

X Z Zhou

Publications and source records attributed to X Z Zhou.

30 records · Page 2Linked to original sources

[An analysis of YPLL, WYPLL and VYPLL in Guangzhou, 1983-1994].

In order to assess the health status and risk of various diseases in the population of Guangzhou, the surveillance data of death in 1983-1994 in Guangzhou was analyzed by indicesas: year of potential life lost (YPLL), work year of lost (WYPLL) and valued year of potential life lost (VYPLL). It was indicated that both Chinese standardized mortality rates (CSMR) and Chinese standardized rates (CSYPLLR) had been declined from 448.2 x 10(-5) and 53.16/1000 to 398.6 x 10(-5) and 42.29/1000 during 1983-1994, respectively. It was suggested that the health status of inhabitants in Guangzhou had been gradually improved. Cancer lesion and poisoning, cardiovascular diseases rank top in CSYPLLR, were the most important diseases affecting life span of the inhabitants. Lesion and poisoning, infectious disease, psychotic disease, ranked the first in Chinese tandardized WYPLL rates (CSWYPLLR) and Chinese standardized VYPLL rates (CSVYPLLR), were important factors that periled the society labor force and economic development. By comparison of sex, both CSMR and CSYPLLR were higher in male than in female (u = 14.76, P < 0.01; u = 27.05, P < 0.01, respectively). Although both values of CSWYPLLR and CSVYPLLR were negative, they were still higher in male than in female. The zero-age-group was far more higher than all the other age groups in CSPLLR, CSWYPLLR and CSVYPLLR.

Adolescent↗

Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins.

The translational friction coefficients and intrinsic viscosities of four proteins (ribonuclease A, lysozyme, myoglobin, and chymotrypsinogen A) are calculated using atomic-level structural details. Inclusion of a 0.9-A-thick hydration shell allows calculated results for both hydrodynamic properties of each protein to reproduce experimental data. The use of detailed protein structures is made possible by relating translational friction and intrinsic viscosity to capacitance and polarizability, which can be calculated easily. The 0.9-A hydration shell corresponds to a hydration level of 0.3-0.4 g water/g protein. Hydration levels within this narrow range are also found by a number of other techniques such as nuclear magnetic resonance spectroscopy, infrared spectroscopy, calorimetry, and computer simulation. The use of detailed protein structures in predicting hydrodynamic properties thus allows hydrodynamic measurement to join the other techniques in leading to a unified picture of protein hydration. In contrast, earlier interpretations of hydrodynamic data based on modeling proteins as ellipsoids gave hydration levels that varied widely from protein to protein and thus challenged the existence of a unified picture of protein hydration.

Algorithms↗